› 2moz

Solution NMR

Structure of the Membrane Protein MerF, a Bacterial Mercury Transporter, Improved by the Inclusion of Chemical Shift Anisotropy Constraints

Released:
DOI: 10.2210/pdb2moz/pdb
PDB entry 2moz coloured by chain, ensemble of 10 models, front view.
PDB entry 2moz coloured by chain, ensemble of 10 models, side view.
PDB entry 2moz coloured by chain, ensemble of 10 models, top view.
Source organism: Morganella morganii
Primary publication:
Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints.
Tian Y, Lu GJ, Marassi FM, Opella SJ
J Biomol NMR 60 67-71 (2014)
PMID: 25103921

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176373 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mercury resistance system transport protein MerF Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 8.67 KDa
Source organism: Morganella morganii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56446 (Residues: 1-81; Coverage: 100%)
Gene names: N0392_16430, OSC06_21060, merF
Sequence domains: Membrane transport protein MerF
Structure domains: bacterial mercury transporter, merf

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 18%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Applications of NMR to membrane proteins.
Opella et al. (2017)
2 more

2 mentions without citation

Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints.
Tian et al. (2014)
1 more